메뉴 건너뛰기




Volumn 19, Issue 12, 2008, Pages 5279-5288

Ribosome-associated complex binds to ribosomes in close proximity of Rpl31 at the exit of the polypeptide tunnel in yeast

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; CHAPERONE; RIBOSOME ASSOCIATED COMPLEX; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 59449099818     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-06-0661     Document Type: Article
Times cited : (73)

References (63)
  • 1
    • 34047124273 scopus 로고    scopus 로고
    • Cold response in Saccharomyces cerevisiae: New functions for old mechanisms
    • Aguilera, J., Randez-Gil, F., and Prieto, J. A. (2007). Cold response in Saccharomyces cerevisiae: new functions for old mechanisms. FEMS Microbiol. Rev. 31, 327-341.
    • (2007) FEMS Microbiol. Rev , vol.31 , pp. 327-341
    • Aguilera, J.1    Randez-Gil, F.2    Prieto, J.A.3
  • 2
    • 0034100041 scopus 로고    scopus 로고
    • Glucose depletion rapidly inhibits translation initiation in yeast
    • Ashe, M. P., De Long, S. K., and Sachs, A. B. (2000). Glucose depletion rapidly inhibits translation initiation in yeast. Mol. Biol. Cell 11, 833-848.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 833-848
    • Ashe, M.P.1    De Long, S.K.2    Sachs, A.B.3
  • 3
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000). The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 4
    • 24744435971 scopus 로고    scopus 로고
    • Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action
    • Baram, D., Pyetan, E., Sittner, A., Auerbach-Nevo, T., Bashan, A., and Yonath, A. (2005). Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. Proc. Natl. Acad. Sci. USA 102, 12017-12022.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12017-12022
    • Baram, D.1    Pyetan, E.2    Sittner, A.3    Auerbach-Nevo, T.4    Bashan, A.5    Yonath, A.6
  • 5
    • 0033942924 scopus 로고    scopus 로고
    • Nonsense-mediated decay mutants do not affect programmed-1 frameshifting
    • Bidou, L., Stahl, G., Hatin, I., Namy, O., Rousset, J. P., and Farabaugh, P. J. (2000). Nonsense-mediated decay mutants do not affect programmed-1 frameshifting. RNA 6, 952-961.
    • (2000) RNA , vol.6 , pp. 952-961
    • Bidou, L.1    Stahl, G.2    Hatin, I.3    Namy, O.4    Rousset, J.P.5    Farabaugh, P.J.6
  • 8
    • 18444383371 scopus 로고    scopus 로고
    • Protein families and RNA recognition
    • Chen, Y., and Varani, G. (2005). Protein families and RNA recognition. FEBS J. 272, 2088-2097.
    • (2005) FEBS J , vol.272 , pp. 2088-2097
    • Chen, Y.1    Varani, G.2
  • 10
    • 36348993862 scopus 로고    scopus 로고
    • Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex
    • Conz, C., Otto, H., Peisker, K., Gautschi, M., Wölfle, T., Mayer, M. P., and Rospert, S. (2007). Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex. J. Biol. Chem. 282, 33977-33984.
    • (2007) J. Biol. Chem , vol.282 , pp. 33977-33984
    • Conz, C.1    Otto, H.2    Peisker, K.3    Gautschi, M.4    Wölfle, T.5    Mayer, M.P.6    Rospert, S.7
  • 11
    • 0034691271 scopus 로고    scopus 로고
    • Yeast ribosomal protein L24 affects the kinetics of protein synthesis and ribosomal protein L39 improves translational accuracy, while mutants lacking both remain viable
    • Dresios, J., Derkatch, I. L., Liebman, S. W., and Synetos, D. (2000). Yeast ribosomal protein L24 affects the kinetics of protein synthesis and ribosomal protein L39 improves translational accuracy, while mutants lacking both remain viable. Biochemistry 39, 7236-7244.
    • (2000) Biochemistry , vol.39 , pp. 7236-7244
    • Dresios, J.1    Derkatch, I.L.2    Liebman, S.W.3    Synetos, D.4
  • 12
    • 0035838497 scopus 로고    scopus 로고
    • Yeast ribosomal protein deletion mutants possess altered peptidyltransferase activity and different sensitivity to cycloheximide
    • Dresios, J., Panopoulos, P., Frantziou, C. P., and Synetos, D. (2001). Yeast ribosomal protein deletion mutants possess altered peptidyltransferase activity and different sensitivity to cycloheximide. Biochemistry 40, 8101-8108.
    • (2001) Biochemistry , vol.40 , pp. 8101-8108
    • Dresios, J.1    Panopoulos, P.2    Frantziou, C.P.3    Synetos, D.4
  • 13
    • 33645467060 scopus 로고    scopus 로고
    • Eukaryotic ribosomal proteins lacking a eubacterial counterpart: Important players in ribosomal function
    • Dresios, J., Panopoulos, P., and Synetos, D. (2006). Eukaryotic ribosomal proteins lacking a eubacterial counterpart: important players in ribosomal function. Mol. Microbiol. 59, 1651-1663.
    • (2006) Mol. Microbiol , vol.59 , pp. 1651-1663
    • Dresios, J.1    Panopoulos, P.2    Synetos, D.3
  • 15
    • 18444378736 scopus 로고    scopus 로고
    • A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes
    • Dudek, J. et al. (2002). A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. EMBO J. 21, 2958-2967.
    • (2002) EMBO J , vol.21 , pp. 2958-2967
    • Dudek, J.1
  • 16
    • 0037277456 scopus 로고    scopus 로고
    • Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae
    • Enyenihi, A. H., and Saunders, W. S. (2003). Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163, 47-54.
    • (2003) Genetics , vol.163 , pp. 47-54
    • Enyenihi, A.H.1    Saunders, W.S.2
  • 17
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • Ferbitz, L., Maier, T., Patzelt, H., Bukau, B., Deuerling, E., and Ban, N. (2004). Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 590-596.
    • (2004) Nature , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 18
    • 0026656122 scopus 로고
    • Spot-synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank, R. (1992). Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 48, 9217-9232.
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 23
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and Sugino, A. (1988). New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 24
    • 0037406142 scopus 로고    scopus 로고
    • The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome
    • Gu, S. Q., Peske, F., Wieden, H. J., Rodnina, M. V., and Wintermeyer, W. (2003). The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome. RNA 9, 566-573.
    • (2003) RNA , vol.9 , pp. 566-573
    • Gu, S.Q.1    Peske, F.2    Wieden, H.J.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 25
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic, M., Becker, T., Pool, M. R., Spahn, C. M., Grassucci, R. A., Frank, J., and Beckmann, R. (2004). Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808-814.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 26
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • Halic, M., Blau, M., Becker, T., Mielke, T., Pool, M. R., Wild, K., Sinning, I., and Beckmann, R. (2006). Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 444, 507-511.
    • (2006) Nature , vol.444 , pp. 507-511
    • Halic, M.1    Blau, M.2    Becker, T.3    Mielke, T.4    Pool, M.R.5    Wild, K.6    Sinning, I.7    Beckmann, R.8
  • 28
    • 0026012156 scopus 로고
    • FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae
    • Heitman, J., Movva, N. R., Hiestand, P. C., and Hall, M. N. (1991). FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 88, 1948-1952.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1948-1952
    • Heitman, J.1    Movva, N.R.2    Hiestand, P.C.3    Hall, M.N.4
  • 29
    • 22444439361 scopus 로고    scopus 로고
    • The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1
    • Huang, P., Gautschi, M., Walter, W., Rospert, S., and Craig, E. A. (2005). The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat. Struct. Mol. Biol. 12, 497-504.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 497-504
    • Huang, P.1    Gautschi, M.2    Walter, W.3    Rospert, S.4    Craig, E.A.5
  • 30
    • 0037007008 scopus 로고    scopus 로고
    • The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain
    • Hundley, H., Eisenman, H., Walter, W., Evans, T., Hotokezaka, Y., Wiedmann, M., and Craig, E. (2002). The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain. Proc. Natl. Acad. Sci. USA 99, 4203-4208.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4203-4208
    • Hundley, H.1    Eisenman, H.2    Walter, W.3    Evans, T.4    Hotokezaka, Y.5    Wiedmann, M.6    Craig, E.7
  • 31
    • 0033829672 scopus 로고    scopus 로고
    • MIDA1 is a sequence specific DNA binding protein with novel DNA binding properties
    • Inoue, T., Shoji, W., and Obinata, M. (2000). MIDA1 is a sequence specific DNA binding protein with novel DNA binding properties. Genes Cells 5, 699-709.
    • (2000) Genes Cells , vol.5 , pp. 699-709
    • Inoue, T.1    Shoji, W.2    Obinata, M.3
  • 33
    • 2942615089 scopus 로고    scopus 로고
    • The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit
    • Klein, D. J., Moore, P. B., and Steitz, T. A. (2004). The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. J. Mol. Biol. 340, 141-177.
    • (2004) J. Mol. Biol , vol.340 , pp. 141-177
    • Klein, D.J.1    Moore, P.B.2    Steitz, T.A.3
  • 34
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: A new RNA secondary structure motif
    • Klein, D. J., Schmeing, T. M., Moore, P. B., and Steitz, T. A. (2001). The kink-turn: a new RNA secondary structure motif. EMBO J. 20, 4214-4221.
    • (2001) EMBO J , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 35
    • 0031602193 scopus 로고    scopus 로고
    • Synthesis and screening of peptide libraries on continuous cellulose membrane supports
    • Kramer, A., and Schneider-Mergener, J. (1998). Synthesis and screening of peptide libraries on continuous cellulose membrane supports. Methods Mol. Biol. 87, 25-39.
    • (1998) Methods Mol. Biol , vol.87 , pp. 25-39
    • Kramer, A.1    Schneider-Mergener, J.2
  • 37
    • 0037115872 scopus 로고    scopus 로고
    • Comparative analysis of ribosomal proteins in complete genomes: An example of reductive evolution at the domain scale
    • Lecompte, O., Ripp, R., Thierry, J. C., Moras, D., and Poch, O. (2002). Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale. Nucleic Acids Res. 30, 5382-5390.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5382-5390
    • Lecompte, O.1    Ripp, R.2    Thierry, J.C.3    Moras, D.4    Poch, O.5
  • 38
    • 33646259466 scopus 로고    scopus 로고
    • Specific effects of ribosome-tethered molecular chaperones on programmed -1 ribosomal frameshifting
    • Muldoon-Jacobs, K. L., and Dinman, J. D. (2006). Specific effects of ribosome-tethered molecular chaperones on programmed -1 ribosomal frameshifting. Eukaryot. Cell 5, 762-770.
    • (2006) Eukaryot. Cell , vol.5 , pp. 762-770
    • Muldoon-Jacobs, K.L.1    Dinman, J.D.2
  • 39
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988). Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 40
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, P. B., and Steitz, T. A. (2000). The structural basis of ribosome activity in peptide bond synthesis. Science 289, 920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 41
    • 0018379922 scopus 로고
    • Phenotypic suppression of nonsense mutants in yeast by aminoglycoside antibiotics
    • Palmer, E., Wilhelm, J. M., and Sherman, F. (1979). Phenotypic suppression of nonsense mutants in yeast by aminoglycoside antibiotics. Nature 277, 148-150.
    • (1979) Nature , vol.277 , pp. 148-150
    • Palmer, E.1    Wilhelm, J.M.2    Sherman, F.3
  • 42
    • 38649122076 scopus 로고    scopus 로고
    • Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes
    • Polevoda, B., Brown, S., Cardillo, T. S., Rigby, S., and Sherman, F. (2008). Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes. J. Cell Biochem. 103, 492-508.
    • (2008) J. Cell Biochem , vol.103 , pp. 492-508
    • Polevoda, B.1    Brown, S.2    Cardillo, T.S.3    Rigby, S.4    Sherman, F.5
  • 43
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • Pool, M. R., Stumm, J., Fulga, T. A., Sinning, I., and Dobberstein, B. (2002). Distinct modes of signal recognition particle interaction with the ribosome. Science 297, 1345-1348.
    • (2002) Science , vol.297 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 44
    • 4744374703 scopus 로고    scopus 로고
    • The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae
    • Rakwalska, M., and Rospert, S. (2004). The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol. Cell. Biol. 24, 9186-9197.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9186-9197
    • Rakwalska, M.1    Rospert, S.2
  • 45
    • 34247281027 scopus 로고    scopus 로고
    • Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence
    • Raue, U., Oellerer, S., and Rospert, S. (2007). Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence. J. Biol. Chem. 282, 7809-7816.
    • (2007) J. Biol. Chem , vol.282 , pp. 7809-7816
    • Raue, U.1    Oellerer, S.2    Rospert, S.3
  • 48
    • 3042555706 scopus 로고    scopus 로고
    • Ribosome function: How to govern the fate of a nascent polypeptide
    • Rospert, S. (2004). Ribosome function: how to govern the fate of a nascent polypeptide. Curr. Biol. 14, R386-R388.
    • (2004) Curr. Biol , vol.14
    • Rospert, S.1
  • 49
    • 84889844014 scopus 로고    scopus 로고
    • Ribosome-bound proteins acting on newly synthesized polypeptide chains
    • eds. J. Buchner and T. Kiefhaber, Weinheim: Wiley-VCH Verlag
    • Rospert, S., Gautschi, M., Rakwalska, M., and Raue, U. (2005a). Ribosome-bound proteins acting on newly synthesized polypeptide chains. In: Protein Folding Handbook, vol. II. eds. J. Buchner and T. Kiefhaber, Weinheim: Wiley-VCH Verlag, 429-458.
    • (2005) Protein Folding Handbook , vol.2 , pp. 429-458
    • Rospert, S.1    Gautschi, M.2    Rakwalska, M.3    Raue, U.4
  • 50
    • 33646849462 scopus 로고    scopus 로고
    • Polypeptide chain termination and stop codon readthrough on eukaryotic ribosomes
    • Rospert, S., Rakwalska, M., and Dubaquié, Y. (2005b). Polypeptide chain termination and stop codon readthrough on eukaryotic ribosomes. Rev. Physiol. Biochem. Pharmacol. 155, 1-30.
    • (2005) Rev. Physiol. Biochem. Pharmacol , vol.155 , pp. 1-30
    • Rospert, S.1    Rakwalska, M.2    Dubaquié, Y.3
  • 52
    • 0029799713 scopus 로고    scopus 로고
    • Organization and characterization of the two yeast ribosomal protein YL19 genes
    • Song, J. M., Cheung, E., and Rabinowitz, J. C. (1996). Organization and characterization of the two yeast ribosomal protein YL19 genes. Curr. Genet. 30, 273-278.
    • (1996) Curr. Genet , vol.30 , pp. 273-278
    • Song, J.M.1    Cheung, E.2    Rabinowitz, J.C.3
  • 53
    • 41949089130 scopus 로고    scopus 로고
    • Yeast life span extension by depletion of 60s ribosomal subunits is mediated by Gcn4
    • Steffen, K. K. et al. (2008). Yeast life span extension by depletion of 60s ribosomal subunits is mediated by Gcn4. Cell 133, 292-302.
    • (2008) Cell , vol.133 , pp. 292-302
    • Steffen, K.K.1
  • 54
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • Steitz, T. A. (2008). A structural understanding of the dynamic ribosome machine. Nat. Rev. Mol. Cell Biol. 9, 242-253.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 242-253
    • Steitz, T.A.1
  • 55
    • 33746526551 scopus 로고    scopus 로고
    • Prediction of RNA binding sites in proteins from amino acid sequence
    • Terribilini, M., Lee, J. H., Yan, C., Jernigan, R. L., Honavar, V., and Dobbs, D. (2006). Prediction of RNA binding sites in proteins from amino acid sequence. RNA 12, 1450-1462.
    • (2006) RNA , vol.12 , pp. 1450-1462
    • Terribilini, M.1    Lee, J.H.2    Yan, C.3    Jernigan, R.L.4    Honavar, V.5    Dobbs, D.6
  • 56
    • 0038360877 scopus 로고    scopus 로고
    • Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome
    • Ullers, R. S., Houben, E. N., Raine, A., ten Hagen-Jongman, C. M., Ehrenberg, M., Brunner, J., Oudega, B., Harms, N., and Luirink, J. (2003). Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome. J. Cell Biol. 161, 679-684.
    • (2003) J. Cell Biol , vol.161 , pp. 679-684
    • Ullers, R.S.1    Houben, E.N.2    Raine, A.3    ten Hagen-Jongman, C.M.4    Ehrenberg, M.5    Brunner, J.6    Oudega, B.7    Harms, N.8    Luirink, J.9
  • 57
    • 33646354930 scopus 로고    scopus 로고
    • A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains
    • Wegrzyn, R. D., Hofmann, D., Merz, F., Nikolay, R., Rauch, T., Graf, C., and Deuerling, E. (2006). A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains. J. Biol. Chem. 281, 2847-2857.
    • (2006) J. Biol. Chem , vol.281 , pp. 2847-2857
    • Wegrzyn, R.D.1    Hofmann, D.2    Merz, F.3    Nikolay, R.4    Rauch, T.5    Graf, C.6    Deuerling, E.7
  • 58
    • 0032419957 scopus 로고    scopus 로고
    • RNA recognition by arginine-rich peptide motifs
    • Weiss, M. A., and Narayana, N. (1998). RNA recognition by arginine-rich peptide motifs. Biopolymers 48, 167-180.
    • (1998) Biopolymers , vol.48 , pp. 167-180
    • Weiss, M.A.1    Narayana, N.2
  • 59
    • 0027933542 scopus 로고
    • Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae
    • Wilhelm, M. L., Reinbolt, J., Gangloff, J., Dirheimer, G., and Wilhelm, F. X. (1994). Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae. FEBS Lett. 349, 260-264.
    • (1994) FEBS Lett , vol.349 , pp. 260-264
    • Wilhelm, M.L.1    Reinbolt, J.2    Gangloff, J.3    Dirheimer, G.4    Wilhelm, F.X.5
  • 60
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler, E. A. et al. (1999). Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285, 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1
  • 61
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • Yaffe, M. P., and Schatz, G. (1984). Two nuclear mutations that block mitochondrial protein import in yeast. Proc. Natl. Acad. Sci. USA. 4819-4823.
    • (1984) Proc. Natl. Acad. Sci. USA , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2
  • 62
    • 0032541489 scopus 로고    scopus 로고
    • Zuotin, a ribosome-associated DnaJ molecular chaperone
    • Yan, W., Schilke, B., Pfund, C., Walter, W., Kim, S., and Craig, E. A. (1998). Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17, 4809-4817.
    • (1998) EMBO J , vol.17 , pp. 4809-4817
    • Yan, W.1    Schilke, B.2    Pfund, C.3    Walter, W.4    Kim, S.5    Craig, E.A.6
  • 63
    • 0026758377 scopus 로고
    • Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae
    • Zhang, S., Lockshin, C., Herbert, A., Winter, E., and Rich, A. (1992). Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae. EMBO J. 11, 3787-3796.
    • (1992) EMBO J , vol.11 , pp. 3787-3796
    • Zhang, S.1    Lockshin, C.2    Herbert, A.3    Winter, E.4    Rich, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.